|
Name |
Accession |
Description |
Interval |
E-value |
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-610 |
0e+00 |
|
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440218 [Multi-domain] Cd Length: 610 Bit Score: 1012.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 1 MCGIVGFVGRDEAAPILLDGLSRLEYRGYDSAGVAVYGaEEGMQVAKAKGRLQVLHDLVKGgSTLHGTIGVGHTRWATHG 80
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLD-DGGLEVRKAVGKLANLEEKLAE-EPLSGTIGIGHTRWATHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 81 APSDVNSHPQVSENGRFAVVHNGIIENYAELREFLQSEGVQFVSDTDTEVAAQLLEYYYQG--NLLEAVVRTLHTIRGAY 158
Cdd:COG0449 79 APSDENAHPHTSCSGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGggDLLEAVRKALKRLEGAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 159 ALGILCADCPDRLIAARKDSPLILGFGDGAHYLASDVTALIKYTREVCWLEDGEIAELTADHLWVYDSYLRPVEKERRHV 238
Cdd:COG0449 159 ALAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVKTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 239 DWEISAAEKGGYEHFMIKEIMEQPEAVRKTISPRIK-DGRVVLDDWGLTARELEEMDRLYVIACGSSYHVGVAAKYILEK 317
Cdd:COG0449 239 DWDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDeDGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 318 LLRKPVEVTLASEFRYCDPIVTEHTLALVISQSGETIDTLAAMREARRLGAKVVSIVNVVGSTIARESDTVLYTWAGPEI 397
Cdd:COG0449 319 LARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 398 AVATTKAYSTQLAVIYLIGLYCADLLGTISRAEYDTILTELQRIPDKLEEILQDREDIQYFATLYFNRHSMFFIGRNLDY 477
Cdd:COG0449 399 GVASTKAFTTQLAALYLLALYLARARGTLSAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGINY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 478 AVGLEGSLKLKEISYIHSEAYAAGELKHGTISLIEPGTLVVALAGCGPLFEKTVSNAVEVKSRGADLLGLTTRDkAAQLG 557
Cdd:COG0449 479 PVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEG-DEEVE 557
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1199604568 558 RTADHVIAIPETHPVLLPSLEVVPMQLFAYYTALQRGCDIDKPRNLAKSVTVE 610
Cdd:COG0449 558 ELADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-610 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 947.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 1 MCGIVGFVGRDEAAPILLDGLSRLEYRGYDSAGVAVYgAEEGMQVAKAKGRLQVLHDLVKGgSTLHGTIGVGHTRWATHG 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVL-DDGGLEVRKAVGKVANLEAKLEE-EPLPGTTGIGHTRWATHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 81 APSDVNSHPQVSENGRFAVVHNGIIENYAELREFLQSEGVQFVSDTDTEVAAQLLEYYYQ--GNLLEAVVRTLHTIRGAY 158
Cdd:PRK00331 79 KPTERNAHPHTDCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKegGDLLEAVRKALKRLEGAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 159 ALGILCADCPDRLIAARKDSPLILGFGDGAHYLASDVTALIKYTREVCWLEDGEIAELTADHLWVYDSYLRPVEKERRHV 238
Cdd:PRK00331 159 ALAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVEREVYTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 239 DWEISAAEKGGYEHFMIKEIMEQPEAVRKTISPRIKDgrvvLDDWGLTARELEEMDRLYVIACGSSYHVGVAAKYILEKL 318
Cdd:PRK00331 239 DWDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRLDE----LGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 319 LRKPVEVTLASEFRYCDPIVTEHTLALVISQSGETIDTLAAMREARRLGAKVVSIVNVVGSTIARESDTVLYTWAGPEIA 398
Cdd:PRK00331 315 AGIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 399 VATTKAYSTQLAVIYLIGLYCADLLGTISRAEYDTILTELQRIPDKLEEILQDREDIQYFATLYFNRHSMFFIGRNLDYA 478
Cdd:PRK00331 395 VASTKAFTAQLAVLYLLALALAKARGTLSAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDYP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 479 VGLEGSLKLKEISYIHSEAYAAGELKHGTISLIEPGTLVVALAGCGPLFEKTVSNAVEVKSRGADLLGLTtrDKAAQLGR 558
Cdd:PRK00331 475 VALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIA--DEGDEVAE 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1199604568 559 TADHVIAIPETHPVLLPSLEVVPMQLFAYYTALQRGCDIDKPRNLAKSVTVE 610
Cdd:PRK00331 553 EADDVIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-610 |
0e+00 |
|
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from Methanococcus jannaschii contains an intein. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]
Pssm-ID: 273462 [Multi-domain] Cd Length: 607 Bit Score: 825.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 2 CGIVGFVGRDEAAPILLDGLSRLEYRGYDSAGVAVygAEEG-MQVAKAKGRLQVLHDLVKGgSTLHGTIGVGHTRWATHG 80
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAV--VDEGkLFVRKAVGKVAELANKLGE-KPLPGGVGIGHTRWATHG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 81 APSDVNSHPQVSENGRFAVVHNGIIENYAELREFLQSEGVQFVSDTDTEVAAQLLEYYYQ--GNLLEAVVRTLHTIRGAY 158
Cdd:TIGR01135 78 KPTDENAHPHTDEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELRegGDLLEAVQKALKQLRGAY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 159 ALGILCADCPDRLIAARKDSPLILGFGDGAHYLASDVTALIKYTREVCWLEDGEIAELTADHLWVYDSYLRPVEKERRHV 238
Cdd:TIGR01135 158 ALAVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 239 DWEISAAEKGGYEHFMIKEIMEQPEAVRKTISPRIKDGRVVLDDwGLTARELEEMDRLYVIACGSSYHVGVAAKYILEKL 318
Cdd:TIGR01135 238 DWDLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEE-LGAEELLKNIDRIQIVACGTSYHAGLVAKYLIERL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 319 LRKPVEVTLASEFRYCDPIVTEHTLALVISQSGETIDTLAAMREARRLGAKVVSIVNVVGSTIARESDTVLYTWAGPEIA 398
Cdd:TIGR01135 317 AGIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 399 VATTKAYSTQLAVIYLIGLYCADLLGTISRAEYDTILTELQRIPDKLEEILQDREDIQYFATLYFNRHSMFFIGRNLDYA 478
Cdd:TIGR01135 397 VASTKAFTTQLTVLYLLALALAKARGTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 479 VGLEGSLKLKEISYIHSEAYAAGELKHGTISLIEPGTLVVALAGCGPLFEKTVSNAVEVKSRGADLLGLTTRDkAAQLGR 558
Cdd:TIGR01135 477 IALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPED-DETIAS 555
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1199604568 559 TADHVIAIPETHPVLLPSLEVVPMQLFAYYTALQRGCDIDKPRNLAKSVTVE 610
Cdd:TIGR01135 556 VADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-609 |
4.37e-170 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 498.39 E-value: 4.37e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 1 MCGIVGFVGRDEAAPILLDGLSRLEYRGYDSAGVAVYGAEEGMQVAKA-------------KGRLQVLHdlvkggstLHG 67
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTISSGGELKTTKYasdgttsdsieilKEKLLDSH--------KNS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 68 TIGVGHTRWATHGAPSDVNSHPQVSENGRFAVVHNGIIENYAELREFLQSEGVQFVSDTDTEVAAQLLEYYYQ--GNLLE 145
Cdd:PTZ00295 96 TIGIAHTRWATHGGKTDENAHPHCDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDqgEDFQE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 146 AVVRTLHTIRGAYALGILCADCPDRLIAARKDSPLILGFGDGAHYLASDVTALIKYTREVCWLEDGEIAELTADHLWVYD 225
Cdd:PTZ00295 176 AVKSAISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLENVNDLY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 226 SyLRPVEKErrhvDWEISAAEKGGYEHFMIKEIMEQPEAVRKTISPRIK----DGRVVLDDWGLTARELEEMDRLYVIAC 301
Cdd:PTZ00295 256 T-QRRVEKI----PEEVIEKSPEPYPHWTLKEIFEQPIALSRALNNGGRlsgyNNRVKLGGLDQYLEELLNIKNLILVGC 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 302 GSSYHVGVAAKYILEKL-LRKPVEVTLASEF-RYCDPivTEHTLALVISQSGETIDTLAAMREARRLGAKVVSIVNVVGS 379
Cdd:PTZ00295 331 GTSYYAALFAASIMQKLkCFNTVQVIDASELtLYRLP--DEDAGVIFISQSGETLDVVRALNLADELNLPKISVVNTVGS 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 380 TIARESDTVLYTWAGPEIAVATTKAYSTQLAVIYLIGLYCA---DLLGTISRAEydTILTELQRIPDKLEEILQDREDI- 455
Cdd:PTZ00295 409 LIARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAqnkEYSCSNYKCS--SLINSLHRLPTYIGMTLKSCEEQc 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 456 QYFATLYFNRHSMFFIGRNLDYAVGLEGSLKLKEISYIHSEAYAAGELKHGTISLIEP--GTLVVALAGCGPLFEKTVSN 533
Cdd:PTZ00295 487 KRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKekNTPVILIILDDEHKELMINA 566
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199604568 534 AVEVKSRGADLLGLTtrDKAAQLGRTADHVIAIPETHPvLLPSLEVVPMQLFAYYTALQRGCDIDKPRNLAKSVTV 609
Cdd:PTZ00295 567 AEQVKARGAYIIVIT--DDEDLVKDFADEIILIPSNGP-LTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-610 |
3.70e-147 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 441.11 E-value: 3.70e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 1 MCGIVGFVG------RDEAAPILLDGLSRLEYRGYDSAGVAV--YGAEEGMQ--VAKAKGRLQVLHDLVKGGST---LHG 67
Cdd:PLN02981 1 MCGIFAYLNynvpreRRFILEVLFNGLRRLEYRGYDSAGIAIdnDPSLESSSplVFREEGKIESLVRSVYEEVAetdLNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 68 T------IGVGHTRWATHGAPSDVNSHPQVSENG-RFAVVHNGIIENYAELREFLQSEGVQFVSDTDTEVAAQLLEYYYQ 140
Cdd:PLN02981 81 DlvfenhAGIAHTRWATHGPPAPRNSHPQSSGPGnEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFVFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 141 -----------GNLLEAVVRTLHtirGAYALGILCADCPDRLIAARKDSPLILGFGDGAH-------------------- 189
Cdd:PLN02981 161 klneeegdvtfSQVVMEVMRQLE---GAYALIFKSPHYPNELVACKRGSPLLLGVKELPEeknssavftsegfltknrdk 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 190 ----YLASDVTALIKYTREVCWLEDGEIAEL----------TADHLWVYDSYLRPVEKER--RHVDWEISAAEKGGYEHF 253
Cdd:PLN02981 238 pkefFLASDASAVVEHTKRVLVIEDNEVVHLkdggvgiykfENEKGRGGGGLSRPASVERalSTLEMEVEQIMKGNYDHY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 254 MIKEIMEQPEAVRKTISPRIKDG------RVVLD---DWGLTARELEemdRLYVIACGSSYHVGVAAKYILEKLLRKPVE 324
Cdd:PLN02981 318 MQKEIHEQPESLTTTMRGRLIRGgsgkakRVLLGglkDHLKTIRRSR---RIVFIGCGTSYNAALAARPILEELSGVPVT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 325 VTLASEF--RYCdPIVTEHTlALVISQSGETIDTLAAMREARRLGAKVVSIVNVVGSTIARESDTVLYTWAGPEIAVATT 402
Cdd:PLN02981 395 MELASDLldRQG-PIYREDT-AVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVAST 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 403 KAYSTQLAVIYLIGLYCADllGTISRAE-YDTILTELQRIPDKLEEILQDREDIQYFATLYFNRHSMFFIGRNLDYAVGL 481
Cdd:PLN02981 473 KAYTSQIVAMTMLALALGE--DSISSRSrREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNYATAL 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 482 EGSLKLKEISYIHSEAYAAGELKHGTISLIEPGTLVVALAGCGPLFEKTVSNAVEVKSRGADLLGLTTR-DKAAQLGRTA 560
Cdd:PLN02981 551 EGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKgDASSVCPSGG 630
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1199604568 561 DHVIAIPETHPVLLPSLEVVPMQLFAYYTALQRGCDIDKPRNLAKSVTVE 610
Cdd:PLN02981 631 CRVIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-610 |
9.83e-141 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 424.29 E-value: 9.83e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 1 MCGIVGFVGR------DEAAPILLDGLSRLEYRGYDSAGVAV----YGAEEGMQVAKAK----------GRLQVLHDLVK 60
Cdd:PTZ00394 1 MCGIFGYANHnvprtvEQILNVLLDGIQKVEYRGYDSAGLAIdaniGSEKEDGTAASAPtprpcvvrsvGNISQLREKVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 61 GG----------STLHGTIGVGHTRWATHGAPSDVNSHPQVSENGRFAVVHNGIIENYAELREFLQSEGVQFVSDTDTEV 130
Cdd:PTZ00394 81 SEavaatlppmdATTSHHVGIAHTRWATHGGVCERNCHPQQSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 131 AAQLLEYYYQG----NLLEAVVRTLHTIRGAYALGILCADCPDRLIAARKDSPLILGFGDGAH----------------- 189
Cdd:PTZ00394 161 ISVLSEYLYTRkgihNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIRRTDDrgcvmklqtydltdlsg 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 190 ----YLASDVTALIKYTREVCWLEDGEIAELTADHLWVYDSYLRP---VEKERRHVDWEISAAEKGGYEHFMIKEIMEQP 262
Cdd:PTZ00394 241 plevFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQrsiVKREVQHLDAKPEGLSKGNYPHFMLKEIYEQP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 263 EAVRKTISPRIK--DGRVVLDdwGLTA---RELEEMDRLYVIACGSSYHVGVAAKYILEKLLRKPVEVTLASEFRYCDPI 337
Cdd:PTZ00394 321 ESVISSMHGRIDfsSGTVQLS--GFTQqsiRAILTSRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRPR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 338 VTEHTLALVISQSGETIDTLAAMREARRLGAKVVSIVNVVGSTIARESDTVLYTWAGPEIAVATTKAYSTQLAVIYLIGL 417
Cdd:PTZ00394 399 IQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLVAL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 418 YCADLLGTIS--RAEydtILTELQRIPDKLEEILQDRED-IQYFATLYFNRHSMFFIGRNLDYAVGLEGSLKLKEISYIH 494
Cdd:PTZ00394 479 LLSSDSVRLQerRNE---IIRGLAELPAAISECLKITHDpVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYVH 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 495 SEAYAAGELKHGTISLIEPGTLVVALAGCGPLFEKTVSNAVEVKSRGADLLGLTTrDKAAQLGRTADHVIAIPETHPVLL 574
Cdd:PTZ00394 556 TEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFAT-EVDAELKAAASEIVLVPKTVDCLQ 634
|
650 660 670
....*....|....*....|....*....|....*.
gi 1199604568 575 PSLEVVPMQLFAYYTALQRGCDIDKPRNLAKSVTVE 610
Cdd:PTZ00394 635 CVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-216 |
9.12e-119 |
|
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus of glucosamine-6P synthase (GlmS, or GFAT in humans). The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. In humans, GFAT catalyzes the first and rate-limiting step of hexosamine metabolism, the conversion of D-fructose-6P (Fru6P) into D-glucosamine-6P using L-glutamine as a nitrogen source. The end product of this pathway, UDP-N-acetyl glucosamine, is a major building block of the bacterial peptidoglycan and fungal chitin.
Pssm-ID: 238366 [Multi-domain] Cd Length: 215 Bit Score: 351.36 E-value: 9.12e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 2 CGIVGFVGRDEAAPILLDGLSRLEYRGYDSAGVAVYGaEEGMQVAKAKGRLQVLHDLVKGgSTLHGTIGVGHTRWATHGA 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIG-DGSLEVVKAVGKVANLEEKLAE-KPLSGHVGIGHTRWATHGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 82 PSDVNSHPQVSENGRFAVVHNGIIENYAELREFLQSEGVQFVSDTDTEVAAQLLEYYYQGN--LLEAVVRTLHTIRGAYA 159
Cdd:cd00714 79 PTDVNAHPHRSCDGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGldLLEAVKKALKRLEGAYA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199604568 160 LGILCADCPDRLIAARKDSPLILGFGDGAHYLASDVTALIKYTREVCWLEDGEIAEL 216
Cdd:cd00714 159 LAVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
256-610 |
9.57e-79 |
|
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441824 [Multi-domain] Cd Length: 336 Bit Score: 252.51 E-value: 9.57e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 256 KEIMEQPEAVRKTISprikDGRVVLDDWGLTARELEEmDRLYVIACGSSYHVGVAAKYILEKLLRKPVEVTLASEF-RYC 334
Cdd:COG2222 2 REIAQQPEAWRRALA----ALAAAIAALLARLRAKPP-RRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELvVYP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 335 DPIVTEHTLALVISQSGETIDTLAAMREARRLGAKVVSIVNVVGSTIARESDTVLYTWAGPEIAVATTKAYSTQLAVIYL 414
Cdd:COG2222 77 AYLKLEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLALLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 415 I-GLYCADllgtisraeyDTILTELQRIPDKLEEILQDREDIQYFATLyFNRHSMFFIGRNLDYAVGLEGSLKLKEISYI 493
Cdd:COG2222 157 LlAAWGGD----------DALLAALDALPAALEAALAADWPAAALAAL-ADAERVVFLGRGPLYGLAREAALKLKELSAG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 494 HSEAYAAGELKHGTISLIEPGTLVVALAGCGPLFEKTVSNAVEVKSRGADLLGLTTRDKAaqlgrtADHVIAIPETHPVL 573
Cdd:COG2222 226 HAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDA------AITLPAIPDLHDAL 299
|
330 340 350
....*....|....*....|....*....|....*..
gi 1199604568 574 LPSLEVVPMQLFAYYTALQRGCDIDKPRNLAKSVTVE 610
Cdd:COG2222 300 DPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-214 |
1.45e-61 |
|
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.
Pssm-ID: 238212 [Multi-domain] Cd Length: 220 Bit Score: 203.45 E-value: 1.45e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 2 CGIVGFVGRDEAAPILLD----GLSRLEYRGYDSAGVAVYGAEEGMQVAKAKGRLQVLHDLVKggSTLHGTIGVGHTRWA 77
Cdd:cd00352 1 CGIFGIVGADGAASLLLLlllrGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLLD--EPLKSGVALGHVRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 78 THGAPSDVNSHPQVSENGRFAVVHNGIIENYAELREFLQSEGVQFVSDTDTEVAAQLLE-YYYQGNLLEAVVRTLHTIRG 156
Cdd:cd00352 79 TNGLPSEANAQPFRSEDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLErLGREGGLFEAVEDALKRLDG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199604568 157 AYALGILCADcPDRLIAARK---DSPLILGFG-DGAHYLASDVTALIKYT-REVCWLEDGEIA 214
Cdd:cd00352 159 PFAFALWDGK-PDRLFAARDrfgIRPLYYGITkDGGLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
295-420 |
8.14e-60 |
|
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.
Pssm-ID: 240141 [Multi-domain] Cd Length: 126 Bit Score: 195.41 E-value: 8.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 295 RLYVIACGSSYHVGVAAKYILEKLLRKPVEVTLASEFRYCDPIVTEHTLALVISQSGETIDTLAAMREARRLGAKVVSIV 374
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1199604568 375 NVVGSTIARESDTVLYTWAGPEIAVATTKAYSTQLAVIYLIGLYCA 420
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
453-608 |
5.55e-58 |
|
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.
Pssm-ID: 240142 [Multi-domain] Cd Length: 153 Bit Score: 191.32 E-value: 5.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 453 EDIQYFATLYFNRHSMFFIGRNLDYAVGLEGSLKLKEISYIHSEAYAAGELKHGTISLIEPGTLVVALAGCGPLFEKTVS 532
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199604568 533 NAVEVKSRGADLLGLTTrdkAAQLGRTADHVIAIPETHPVLLPSLEVVPMQLFAYYTALQRGCDIDKPRNLAKSVT 608
Cdd:cd05009 81 LIKEVKARGAKVIVITD---DGDAKDLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-237 |
2.17e-43 |
|
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the N-terminus of glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase) . The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. GPATase crystalizes as a homotetramer, but can also exist as a homdimer.
Pssm-ID: 238367 [Multi-domain] Cd Length: 252 Bit Score: 155.70 E-value: 2.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 2 CGIVGFVGRDEAAPILLDGLSRLEYRGYDSAGVAVYGAEEgMQVAKAKGRL-QVLHDLVKggSTLHGTIGVGHTRWATHG 80
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGKR-FHTHKGMGLVsDVFDEEKL--RRLPGNIAIGHVRYSTAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 81 APSDVNSHPQVSE--NGRFAVVHNGIIENYAELREFLQSEGVQFVSDTDTEVAAQLLEYYYQ-GNLLEAVVRTLHTIRGA 157
Cdd:cd00715 78 SSSLENAQPFVVNspLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAkDDLFEAIIDALERVKGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 158 YALGILcadCPDRLIAARkDS----PLILG-FGDGAHYLASDVTAL----IKYTREVcwlEDGEIAELTADHLwvyDSYL 228
Cdd:cd00715 158 YSLVIM---TADGLIAVR-DPhgirPLVLGkLEGDGYVVASESCALdiigAEFVRDV---EPGEIVVIDDDGL---ESSQ 227
|
....*....
gi 1199604568 229 RPVEKERRH 237
Cdd:cd00715 228 RAPKPKPAP 236
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-237 |
6.33e-42 |
|
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; Glutamine phosphoribosylpyrophosphate amidotransferase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439804 [Multi-domain] Cd Length: 464 Bit Score: 157.49 E-value: 6.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 1 MCGIVGFVGRDEAAPILLDGLSRLEYRGYDSAGVAVYGAEEgMQVAKAKGRL-QVLHDlvKGGSTLHGTIGVGHTRWATH 79
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSDGGR-FHLHKGMGLVsDVFDE--EDLERLKGNIAIGHVRYSTT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 80 GAPSDVNSHPQV--SENGRFAVVHNGIIENYAELREFLQSEGVQFVSDTDTEVAAQLL-EYYYQGNLLEAVVRTLHTIRG 156
Cdd:COG0034 84 GSSSLENAQPFYvnSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIaRELTKEDLEEAIKEALRRVKG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 157 AYALGILcadCPDRLIAARkDS----PLILGFGDGAHYLASDVTAL----IKYTREVcwlEDGEIAELTADHLwvyDSYl 228
Cdd:COG0034 164 AYSLVIL---TGDGLIAAR-DPngirPLVLGKLEDGYVVASESCALdilgAEFVRDV---EPGEIVVIDEDGL---RSR- 232
|
....*....
gi 1199604568 229 RPVEKERRH 237
Cdd:COG0034 233 QFAEKPRPA 241
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-222 |
1.62e-33 |
|
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273461 [Multi-domain] Cd Length: 442 Bit Score: 133.21 E-value: 1.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 2 CGIVGFVGRDEAAPILL-DGLSRLEYRGYDSAGVAVYGAEEgMQVAKAKGRL-QVLHDlvKGGSTLHGTIGVGHTRWATH 79
Cdd:TIGR01134 1 CGVVGIYGQEEVAASLTyYGLYALQHRGQESAGISVFDGNR-FRLHKGNGLVsDVFNE--EHLQRLKGNVGIGHVRYSTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 80 GAPSDVNSHPQV--SENGRFAVVHNGIIENYAELREFLQSEGVQFVSDTDTEVAAQLLEYYYQGN--LLEAVVRTLHTIR 155
Cdd:TIGR01134 78 GSSGLENAQPFVvnSPYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKddLFDAVARVLERVR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199604568 156 GAYALGILcadCPDRLIAARkDS----PLILGFGDGAHYLASDVTAL----IKYTREVcwlEDGEIAELTADHLW 222
Cdd:TIGR01134 158 GAYALVLM---TEDGLVAVR-DPhgirPLVLGRRGDGYVVASESCALdilgAEFVRDV---EPGEVVVIFDGGLE 225
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
289-414 |
2.74e-31 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 118.17 E-value: 2.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 289 ELEEMDRLYVIACGSSYHVGVAAKYILEKLLRKPVEVTLASEFRY-CDPIVTEHTLALVISQSGETIDTLAAMREARRLG 367
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHgVLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1199604568 368 AKVVSIVNVVGSTIARESDTVLYTWAGPEIAVATTKAYSTQLAVIYL 414
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDA 127
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-213 |
1.08e-29 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 122.45 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 2 CGIVGFVGRD--EAAPILLDGLSRLEYRGYDSAGVAVYGAEEgMQVAKAKGRLQVL--HDLVKGgstLHGTIGVGHTRWA 77
Cdd:PRK05793 15 CGVFGVFSKNniDVASLTYYGLYALQHRGQESAGIAVSDGEK-IKVHKGMGLVSEVfsKEKLKG---LKGNSAIGHVRYS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 78 THGAPSDVNSHPQVSE--NGRFAVVHNGIIENYAELREFLQSEGVQFVSDTDTEVAAQLLEYYYQGNLLEAVVRTLHTIR 155
Cdd:PRK05793 91 TTGASDLDNAQPLVANykLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAKKGLEKALVDAIQAIK 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199604568 156 GAYALGILCAdcpDRLIAARKDS---PLILGFGDGAHYLASDVTAL----IKYTREVcwlEDGEI 213
Cdd:PRK05793 171 GSYALVILTE---DKLIGVRDPHgirPLCLGKLGDDYILSSESCALdtigAEFIRDV---EPGEI 229
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-221 |
9.97e-26 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 110.92 E-value: 9.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 1 MCGIVGFVGRDEAAPILLDGLSRLEYRGYDSAGVavygaeegmqVAKAKGRLQVLHD--LVK------GGSTLHGTIGVG 72
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGI----------VTVDGNRLQSITGngLVSdvfdesKLDQLPGDIAIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 73 HTRWATHGAPSDVNSHPQV--SENGRFAVVHNGIIENYAELREFLQSEGVQFVSDTDTEVAAQLLEYYYQGNLLEAVVRT 150
Cdd:PLN02440 71 HVRYSTAGASSLKNVQPFVanYRFGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKARPFFSRIVDA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199604568 151 LHTIRGAYALGILCAdcpDRLIAARKDS---PLILGF-GDGAHYLASDVTAL----IKYTREVCwleDGEIAELTADHL 221
Cdd:PLN02440 151 CEKLKGAYSMVFLTE---DKLVAVRDPHgfrPLVMGRrSNGAVVFASETCALdligATYEREVN---PGEVIVVDKDKG 223
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
66-194 |
2.67e-23 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.
Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 95.45 E-value: 2.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 66 HGTIGVGHTRWATHGAPSDVNsHPQVSENGRFAVVHNGIIENYAELREFLQSEGVQFVSDTDTEVAAQLLEYYyqGnlle 145
Cdd:pfam13522 9 EGGVALGHVRLAIVDLPDAGN-QPMLSRDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYEEW--G---- 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1199604568 146 avVRTLHTIRGAYALGIlcADC-PDRLIAARKD---SPLILGFGDGAHYLASD 194
Cdd:pfam13522 82 --EDCLERLRGMFAFAI--WDRrRRTLFLARDRlgiKPLYYGILGGGFVFASE 130
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-213 |
2.73e-23 |
|
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238888 [Multi-domain] Cd Length: 249 Bit Score: 99.26 E-value: 2.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 2 CGIVGFVGRDEA---APILLDGLSRLEYRG-YDSAGVAVYGAEEG--------MQVAKAKGRLQvlhDLVK--GGSTLHG 67
Cdd:cd01907 1 CGIFGIMSKDGEpfvGALLVEMLDAMQERGpGDGAGFALYGDPDAfvyssgkdMEVFKGVGYPE---DIARryDLEEYKG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 68 TIGVGHTRWATHGAPSDVNSHPQVSENgrFAVVHNGIIENYAELREFLQSEGVQFVSDTDTEVAAQLLEYYY--QGNLLE 145
Cdd:cd01907 78 YHWIAHTRQPTNSAVWWYGAHPFSIGD--IAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLrkGGLPLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 146 AVVRT----------LHTIRGAYALGILcaDCPDRLIAARKDS-----------PLILGFGDGAHYLASDVTALikytRE 204
Cdd:cd01907 156 YYKHIirmpeeerelLLALRLTYRLADL--DGPFTIIVGTPDGfivirdriklrPAVVAETDDYVAIASEECAI----RE 229
|
....*....
gi 1199604568 205 VCWLEDGEI 213
Cdd:cd01907 230 IPDRDNAKV 238
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
461-591 |
1.54e-22 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 93.52 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 461 LYFNRHSMFFIGRNLDYAVGLEGSLKLKEISYIHSEAYAAGELKHGTISLIEPGTLVVALAGCGPLFEkTVSNAVEVKSR 540
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKD-LLAAAELAKAR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1199604568 541 GADLLGLTTRdKAAQLGRTADHVIAIPETHPVLLPSLEVVPMQLFAYYTAL 591
Cdd:pfam01380 80 GAKIIAITDS-PGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALA 129
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-200 |
8.64e-19 |
|
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia.
Pssm-ID: 238364 [Multi-domain] Cd Length: 220 Bit Score: 85.30 E-value: 8.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 2 CGIVGFVGRD---EAAPILLDGLSRLEYRGYDSAGVAVygaeegmqvakakgrlqvlhdlvkggstlHGTIGVGHTRWA- 77
Cdd:cd00712 1 CGIAGIIGLDgasVDRATLERMLDALAHRGPDGSGIWI-----------------------------DEGVALGHRRLSi 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 78 ---THGApsdvnsHPQVSENGRFAVVHNGIIENYAELREFLQSEGVQFVSDTDTEVAAQLLEYYyqGnlleavVRTLHTI 154
Cdd:cd00712 52 idlSGGA------QPMVSEDGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHLYEEW--G------EDCLERL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1199604568 155 RGAYALGILCADcPDRLIAAR-----KdsPLILGFGDGAHYLASDVTALIK 200
Cdd:cd00712 118 NGMFAFALWDKR-KRRLFLARdrfgiK--PLYYGRDGGGLAFASELKALLA 165
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-201 |
2.25e-18 |
|
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis
Pssm-ID: 440136 [Multi-domain] Cd Length: 558 Bit Score: 88.74 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 1 MCGIVGFVGRDEAA--PILLDGLSRLEYRGYDSAGVAVygaeegmqvakakgrlqvlhdlvkggstlHGTIGVGHTR--- 75
Cdd:COG0367 1 MCGIAGIIDFDGGAdrEVLERMLDALAHRGPDGSGIWV-----------------------------DGGVALGHRRlsi 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 76 --WATHGApsdvnsHPQVSENGRFAVVHNGIIENYAELREFLQSEGVQFVSDTDTEVAAQLLEYYyqGnllEAVVRTLht 153
Cdd:COG0367 52 idLSEGGH------QPMVSEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAYEEW--G---EDCLERL-- 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1199604568 154 iRGAYALGILCADCpDRLIAAR-----KdsPLILGFGDGAHYLASDVTALIKY 201
Cdd:COG0367 119 -NGMFAFAIWDRRE-RRLFLARdrfgiK--PLYYAEDGGGLAFASELKALLAH 167
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
92-198 |
9.06e-17 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase.
Pssm-ID: 433289 [Multi-domain] Cd Length: 123 Bit Score: 76.79 E-value: 9.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 92 SENGRFAVVHNGIIENYAELREFLQSEGVQFVSDTDTEVAAQLLEYYYqgnlLEAVVRTLhtiRGAYALGILCADCpDRL 171
Cdd:pfam13537 19 SEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAEW----GEDCVDRL---NGMFAFAIWDRRR-QRL 90
|
90 100 110
....*....|....*....|....*....|...
gi 1199604568 172 IAAR-----KdsPLILGFGDGAHYL-ASDVTAL 198
Cdd:pfam13537 91 FLARdrfgiK--PLYYGRDDGGRLLfASELKAL 121
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
286-415 |
1.23e-16 |
|
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many phosphosugar isomerases and phosphosugar binding proteins. In E. coli, rpiR negatively regulates the expression of rpiB gene. Both rpiB and rpiA are ribose phosphate isomerases that catalyze the reversible reactions of ribose 5-phosphate into ribulose 5-phosphate.
Pssm-ID: 240144 [Multi-domain] Cd Length: 139 Bit Score: 76.88 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 286 TARELEEMDRLYVIACGSSYHVGVAAKYILEKLLRKPVEVTLASEFRYCDPIVTEHTLALVISQSGETIDTLAAMREARR 365
Cdd:cd05013 6 AVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAAEIAKE 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1199604568 366 LGAKVVSIVNVVGSTIARESDTVLYTWAGPEIAVATtkAYSTQLAVIYLI 415
Cdd:cd05013 86 RGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRSS--AFSSRIAQLALI 133
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
294-455 |
1.25e-14 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 74.58 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 294 DRLYVIACGSSYHVGVAAKYILEKLlRKPVEV------TLASEFRycdpIVTEHTLALVISQSGETIDTLAAMREARRLG 367
Cdd:COG1737 135 RRIYIFGVGASAPVAEDLAYKLLRL-GKNVVLldgdghLQAESAA----LLGPGDVVIAISFSGYTRETLEAARLAKERG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 368 AKVVSIVNVVGSTIARESDTVLYTWAgpEIAVATTKAYSTQLAVIYLIglycadllgtisraeyDTILTEL-QRIPDKLE 446
Cdd:COG1737 210 AKVIAITDSPLSPLAKLADVVLYVPS--EEPTLRSSAFSSRVAQLALI----------------DALAAAVaQRDGDKAR 271
|
....*....
gi 1199604568 447 EILQDREDI 455
Cdd:COG1737 272 ERLERTEAL 280
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
295-411 |
2.09e-14 |
|
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240214 [Multi-domain] Cd Length: 120 Bit Score: 69.91 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 295 RLYVIACGSSYHVGVAAKYILEKLLRKPVEVTLASEFRYCDPI-VTEHTLALVISQSGETIDTLAAMREARRLGAKVVSI 373
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKrLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1199604568 374 VNVVGSTIARESDTVLYTwaGPEIAVATTK-AYSTQLAV 411
Cdd:cd05710 81 TDDEDSPLAKLADYVIVY--GFEIDAVEEKyLLLYMLAL 117
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-240 |
6.83e-11 |
|
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 64.66 E-value: 6.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 4 IVGFVGRDEAAPILLDGLSR----LEYRGYDSAGVaVYGaeegmqvakakgrlqvlhdlvkggstlHGTIGVGHTRWATh 79
Cdd:TIGR01536 1 IAGFFDLDDKAVEEDEAIKRmsdtIAHRGPDASGI-EYK---------------------------DGNAILGHRRLAI- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 80 gapSDVNSHPQ--VSENGRFAVVHNGIIENYAELREFLQSEGVQFVSDTDTEVAAQLLEYYyqGnlleavVRTLHTIRGA 157
Cdd:TIGR01536 52 ---IDLSGGAQpmSNEGKTYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHLYEEW--G------EECVDRLDGM 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 158 YALGILCADcpDRLIAARKD----SPLILGFGDGAHYLASDVTALIKytreVCWLEdgeiAELTADHLWVYDSYLRPVEK 233
Cdd:TIGR01536 121 FAFALWDSE--KGELFLARDrfgiKPLYYAYDGGQLYFASEIKALLA----HPNIK----PFPDGAALAPGFGFVRVPPP 190
|
....*..
gi 1199604568 234 ERRHVDW 240
Cdd:TIGR01536 191 STFFRGV 197
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-198 |
8.55e-11 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 64.74 E-value: 8.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 1 MCGIVGFVG----RDEAAPILLDGLSRLEYRGYDSAGVAVYGAEEGMQVAKAKGRLQVLhDLVKGgstlhgtigvghtrw 76
Cdd:PTZ00077 1 MCGILAIFNskgeRHELRRKALELSKRLRHRGPDWSGIIVLENSPGTYNILAHERLAIV-DLSDG--------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 77 athgapsdvnSHPQVSENGRFAVVHNGIIENYAELREFLQSEGVQFVSDTDTEVAAQLLEYYYQGNLleavvrtLHTIRG 156
Cdd:PTZ00077 65 ----------KQPLLDDDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKEYGPKDF-------WNHLDG 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1199604568 157 AYAlGILCADCPDRLIAARKD---SPLILGFG-DGAHYLASDVTAL 198
Cdd:PTZ00077 128 MFA-TVIYDMKTNTFFAARDHigiIPLYIGYAkDGSIWFSSELKAL 172
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
253-601 |
4.14e-10 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 61.56 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 253 FMIKEIMEQpeAVRKTISPRIKDGRVVLDDwgLTARELeemDRLYVIACGSSYHVGVAAKYILEKLlrKPVEVTLASEFR 332
Cdd:PRK11382 11 FLVTENMVQ--EVEKVLSHDVPLVHAIVEE--MVKRDI---DRIYFVACGSPLNAAQTAKHLADRF--SDLQVYAISGWE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 333 YCD--PIVTEHTLALV-ISQSGETIDTLAAMREARRLGAKVVSIVNVVGSTIARESDTVLYTWAGPEIAVATTKAYSTQL 409
Cdd:PRK11382 82 FCDntPYRLDDRCAVIgVSDYGKTEEVIKALELGRACGALTAAFTKRADSPITSAAEFSIDYQADCIWEIHLLLCYSVVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 410 AVIYLIGlycadllgtiSRAEYDTILTELQRIPDKLEEILQDREDIQYFATLYFNRHSMFFIG-----RNLDYAvglEGS 484
Cdd:PRK11382 162 EMITRLA----------PNAEIGKIKNDLKQLPNALGHLVRTWEEKGRQLGELASQWPMIYTVaagplRPLGYK---EGI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 485 LKLKEISYIHSEAYAAGELKHGTISLIEPGTLVVALAGCGPLFEKTVSNAVEVKSRGADLLGLTTRDKAAQLgrtadhvi 564
Cdd:PRK11382 229 VTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDESRHTTERAINFVKQRTDNVIVIDYAEISQGL-------- 300
|
330 340 350
....*....|....*....|....*....|....*..
gi 1199604568 565 aipetHPVLLPSLEVVPMQLFAYYTALQRGCDIDKPR 601
Cdd:PRK11382 301 -----HPWLAPFLMFVPMEWLCYYLSIYKDHNPDERR 332
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
1-175 |
7.29e-10 |
|
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine amidotransferase-like protein of unknown function found in prokaryotes, eukaryotes and archaea. YafJ has a conserved structural fold similar to those of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The YafJ fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238889 [Multi-domain] Cd Length: 257 Bit Score: 60.10 E-value: 7.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 1 MCGIVGFVGrdeaAPILLDGL------SRLEYRGY----------DSAGVAVYGAEEGmQVAKAKGRLQVLHDLVKG--G 62
Cdd:cd01908 1 MCRLLGYSG----APIPLEPLlirpshSLLVQSGGpremkgtvhaDGWGIGWYEGKGG-RPFRYRSPLPAWSDINLEslA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 63 STLHGTIGVGHTRWATHGAPSDVNSHPQVSENGRFAvvHNGIIENYAELR-EFLQSEGVQFVSDTDTEVA-----AQLLE 136
Cdd:cd01908 76 RPIKSPLVLAHVRAATVGPVSLENCHPFTRGRWLFA--HNGQLDGFRLLRrRLLRLLPRLPVGTTDSELAfalllSRLLE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1199604568 137 YYYQG--NLLEAVVRTLHTIRGAYALGILC---ADcPDRLIAAR 175
Cdd:cd01908 154 RDPLDpaELLDAILQTLRELAALAPPGRLNlllSD-GEYLIATR 196
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-198 |
2.53e-09 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 60.16 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 1 MCGIVGFVGRDEAAP---ILLDGLS-RLEYRGYDSAGVAVYGAEegmqvakakgrlqvlhdlvkggstlhgtiGVGHTRW 76
Cdd:PLN02549 1 MCGILAVLGCSDDSQakrSRVLELSrRLRHRGPDWSGLYGNEDC-----------------------------YLAHERL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 77 ATHGAPSdvNSHPQVSENGRFAVVHNGIIENYAELREFLQSegVQFVSDTDTEVAAQLLEYYyqGnllEAVVRTLhtiRG 156
Cdd:PLN02549 52 AIMDPES--GDQPLYNEDKTIVVTANGEIYNHKELREKLKL--HKFRTGSDCEVIAHLYEEH--G---EEFVDML---DG 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1199604568 157 AYALgILCADCPDRLIAARKD---SPLILGFG-DGAHYLASDVTAL 198
Cdd:PLN02549 120 MFSF-VLLDTRDNSFIAARDHigiTPLYIGWGlDGSVWFASEMKAL 164
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
337-389 |
1.76e-08 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 56.31 E-value: 1.76e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1199604568 337 IVTEHTLALVISQSGETIDTLAAMREARRLGAKVVSIVNVVGSTIARESDTVL 389
Cdd:PRK11337 184 LLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVI 236
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-205 |
1.36e-07 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 54.53 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 1 MCGIVGFVGRDEAAPIL----LDGLSRLEYRGYDSAGVavygaeegmqVAKAKGRLqvlhdlvkggstlhgtigvGHTRW 76
Cdd:PRK09431 1 MCGIFGILDIKTDADELrkkaLEMSRLMRHRGPDWSGI----------YASDNAIL-------------------GHERL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 77 AThgapSDVNS--HPQVSENGRFAVVHNGIIENYAELREFLQSeGVQFVSDTDTEVaaqLLEYYYqgnllEAVVRTLHTI 154
Cdd:PRK09431 52 SI----VDVNGgaQPLYNEDGTHVLAVNGEIYNHQELRAELGD-KYAFQTGSDCEV---ILALYQ-----EKGPDFLDDL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199604568 155 RGAYALGILCADcPDRLIAARkDS----PLILGF-GDGAHYLASDVTALIKYTREV 205
Cdd:PRK09431 119 DGMFAFALYDSE-KDAYLIAR-DPigiiPLYYGYdEHGNLYFASEMKALVPVCKTI 172
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
296-374 |
1.97e-07 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 48.91 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 296 LYVIACGSSYHVGVAAKYILEKLLRKPVEVTLASEFRYCDPIV--TEHTLALVISQSGETIDTLAAMREARRLGAKVVSI 373
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSllRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 1199604568 374 V 374
Cdd:cd04795 81 T 81
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
338-397 |
2.13e-06 |
|
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ISomerase) domain. The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. The bacterial cell wall sugar N-acetylmuramic acid carries a unique D-lactyl ether substituent at the C3 position. The etherase catalyzes the cleavage of the lactyl ether bond of N-acetylmuramic acid 6-phosphate.
Pssm-ID: 240140 [Multi-domain] Cd Length: 257 Bit Score: 49.44 E-value: 2.13e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 338 VTEHTLALVISQSGETIDTLAAMREARRLGAKVVSIVNVVGSTIARESDTVLYTWAGPEI 397
Cdd:cd05007 116 LTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEV 175
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
336-390 |
3.36e-05 |
|
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) superfamily. In the ribulose monophosphate pathway of formaldehyde fixation, hexulose-6-phosphate synthase catalyzes the condensation of ribulose-5-phosphate with formadelhyde to become hexulose-6-phosphate, which is then isomerized to fructose-6-phosphate by PHI.
Pssm-ID: 240138 [Multi-domain] Cd Length: 179 Bit Score: 44.87 E-value: 3.36e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1199604568 336 PIVTEHTLALVISQSGETIDTLAAMREARRLGAKVVSIVNVVGSTIARESDTVLY 390
Cdd:cd05005 71 PAIGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVV 125
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
337-396 |
3.39e-05 |
|
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440557 [Multi-domain] Cd Length: 317 Bit Score: 46.12 E-value: 3.39e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 337 IVTEHTLALVISQSGETIDTLAAMREARRLGAKVVSIVNVVGSTIARESDTVLYTWAGPE 396
Cdd:COG0794 88 MITPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVERE 147
|
|
| PRK08674 |
PRK08674 |
bifunctional phosphoglucose/phosphomannose isomerase; Validated |
254-373 |
6.35e-05 |
|
bifunctional phosphoglucose/phosphomannose isomerase; Validated
Pssm-ID: 181536 [Multi-domain] Cd Length: 337 Bit Score: 45.36 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 254 MIKEIMEQPEAVRKTISPRIKDGRVVlddwgltarELEEMDRLYVIACGSSYHVGVAAKYILEKLLRKPVevtlaseFRY 333
Cdd:PRK08674 4 MLEEYLNWPEQFEEALEIAISLDLEE---------DLEKIDNIVISGMGGSGIGGDLLRILLFDELKVPV-------FVN 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1199604568 334 CD----PIVTEHTLALVISQSGETIDTLAAMREARRLGAKVVSI 373
Cdd:PRK08674 68 RDytlpAFVDEKTLVIAVSYSGNTEETLSAVEQALKRGAKIIAI 111
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
347-397 |
1.43e-04 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 44.00 E-value: 1.43e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1199604568 347 ISQSGETIDTLAAMREARRLGAKVVSIVNVVGSTIARESDTVLYTWAGPEI 397
Cdd:PRK05441 138 IAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEV 188
|
|
| GATase_4 |
pfam13230 |
Glutamine amidotransferases class-II; This family captures members that are not found in ... |
65-159 |
4.51e-04 |
|
Glutamine amidotransferases class-II; This family captures members that are not found in pfam00310.
Pssm-ID: 433047 [Multi-domain] Cd Length: 272 Bit Score: 42.32 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199604568 65 LHGTIGVGHTRWATHGAPSDVNSHPQVSE-NGR---FAvvHNGIIENYAElreflQSEGV-QFVSDTDTEVA-AQLL--- 135
Cdd:pfam13230 69 IRSRNVIAHIRKATQGRVTLENTHPFMRElWGRywiFA--HNGDLKGYAP-----KLSGRfQPVGSTDSELAfCWLLdrl 141
|
90 100
....*....|....*....|....*.
gi 1199604568 136 --EYYYQGNLLEAVVRTLHTIRGAYA 159
Cdd:pfam13230 142 asRFPYARPSAGELFRALRELAREIA 167
|
|
| SIS_PGI_PMI_1 |
cd05017 |
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ... |
336-373 |
7.55e-04 |
|
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the phosphoglucose isomerase (PGI) and the phosphomannose isomerase (PMI) functions. These functions catalyze the reversible reactions of glucose 6-phosphate to fructose 6-phosphate, and mannose 6-phosphate to fructose 6-phosphate, respectively at an equal rate. This protein contains two SIS domains. This alignment is based on the first SIS domain.
Pssm-ID: 240148 [Multi-domain] Cd Length: 119 Bit Score: 39.56 E-value: 7.55e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1199604568 336 PIVTEHTLALVISQSGETIDTLAAMREARRLGAKVVSI 373
Cdd:cd05017 39 AFVDRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVAI 76
|
|
| Pgi |
COG0166 |
Glucose-6-phosphate isomerase [Carbohydrate transport and metabolism]; Glucose-6-phosphate ... |
327-366 |
3.18e-03 |
|
Glucose-6-phosphate isomerase [Carbohydrate transport and metabolism]; Glucose-6-phosphate isomerase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439936 Cd Length: 484 Bit Score: 40.51 E-value: 3.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1199604568 327 LASEFRYCDPivtEHTLALVISQSGETIDTLAAMREARRL 366
Cdd:COG0166 148 LAELLAGLDP---ETTLFIVISKSGTTQETLTNARVAREW 184
|
|
| SIS_PGI_1 |
cd05015 |
Phosphoglucose isomerase (PGI) contains two SIS (Sugar ISomerase) domains. This classification ... |
325-366 |
6.17e-03 |
|
Phosphoglucose isomerase (PGI) contains two SIS (Sugar ISomerase) domains. This classification is based on the alignment of the first SIS domain. PGI is a multifunctional enzyme which as an intracellular dimer catalyzes the reversible isomerization of glucose 6-phosphate to fructose 6-phosphate. As an extracellular protein, PGI also has functions equivalent to neuroleukin (NLK), autocrine motility factor (AMF), and maturation factor (MF). Evidence suggests that PGI, NLK, AMF, and MF are closely related or identical. NLK is a neurotrophic growth factor that promotes regeneration and survival of neurons. The dimeric form of NLK has isomerase function, whereas its monomeric form carries out neurotrophic activity. AMF is a cytokine that stimulates cell migration and metastasis. MF mediates the differentiation of human myeloid leukemic HL-60 cells to terminal monocytic cells.
Pssm-ID: 240146 Cd Length: 158 Bit Score: 37.89 E-value: 6.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1199604568 325 VTLASEFRYCDPivtEHTLALVISQSGETIDTLAAMREARRL 366
Cdd:cd05015 61 DDLAELLKKLDP---ETTLFIVISKSGTTLETLANARLAREW 99
|
|
| |
